Hartmut Michel
Max Planck Society
311 Papers
5.8K Citations
Hartmut Michel is an academic researcher from Max Planck Society. The author has contributed to research in topics: Cytochrome c oxidase & Photosynthetic reaction centre. The author has an hindex of 70, co-authored 298 publications. Previous affiliations of Hartmut Michel include University of Texas Southwestern Medical Center & Goethe University Frankfurt.
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Papers
Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans.
Ute Pfitzner,Klaus Hoffmeier,Axel Harrenga,Aimo Kannt,Hartmut Michel,Ernst Bamberg,Oliver-M. H. Richter,Bernd Ludwig +7 more
TL;DR: It is concluded that the D-pathway is too wide in most areas above positions 131/199 to be disturbed by single amino acid replacements, and one of these mutants, N131D, exhibited an ideal decoupled phenotype, with a turnover comparable to that of the wild-type enzyme.
Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS
Jakob Meier-Credo,Laura Preiss,Imke Wüllenweber,Anja Resemann,Christoph Nordmann,Jure Zabret,Detlev Suckau,Hartmut Michel,Marc M. Nowaczyk,Thomas Meier,Julian David Langer +10 more
TL;DR: The MALDI-MS/MS and ISD-based approach can identify and provide valuable sequence information on small membrane proteins, which are inaccessible to conventional Bottom-Up techniques, and is used to unambiguously identify single-point mutations leading to antibiotic resistance in mycobacteria.
Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors
Ye Gao,Bjoern Meyer,Lucie Sokolova,Klaus Zwicker,Michael Karas,Bernd Brutschy,Guohong Peng,Hartmut Michel +7 more
TL;DR: The cytochrome c oxidase Cox2 has been purified from native membranes of the hyperthermophilic eubacterium Aquifex aeolicus and is able to oxidize both reduced cy tochrome c and ubiquinol in a cyanide sensitive manner.
Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis.
Vasundara Srinivasan,Daili J. A. Netz,Holger Webert,Judita Mascarenhas,Antonio J. Pierik,Hartmut Michel,Roland Lill +6 more
TL;DR: The crystal structure of Saccharomyces cerevisiae Cia1 is reported, showing that the WD40 propeller core elements are highly conserved and indicates the conservation of CIA1 function in eukaryotes.
Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus
TL;DR: The "hypothetical protein" Aq_1259 was identified by mass spectrometry and purified from native membranes of Aquifex aeolicus and predicted to be a β-barrel with 16 β-strands, based on the sequence and circular dichroism spectroscopy.